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Development of a proteoliposome model to probe transmembrane electron-transfer reactions.

Biochemical Society transactions (2012-11-28)
Gaye F White, Zhi Shi, Liang Shi, Alice C Dohnalkova, James K Fredrickson, John M Zachara, Julea N Butt, David J Richardson, Thomas A Clarke
RESUMEN

The mineral-respiring bacterium Shewanella oneidensis uses a protein complex, MtrCAB, composed of two decahaem cytochromes brought together inside a transmembrane porin to transport electrons across the outer membrane to a variety of mineral-based electron acceptors. A proteoliposome system has been developed that contains Methyl Viologen as an internalized electron carrier and valinomycin as a membrane-associated cation exchanger. These proteoliposomes can be used as a model system to investigate MtrCAB function.

MATERIALES
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Sigma-Aldrich
Valinomycin, ≥98% (TLC), ≥90% (HPLC)
Supelco
Potassium ionophore I, Selectophore, function tested
Sigma-Aldrich
Valinomycin, ≥99.0% (TLC)
Sigma-Aldrich
Valinomycin, Ready Made Solution, ~1 mg/mL in DMSO